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Conserved domains on  [gi|1845973558|ref|NP_001370799|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
823-975 5.74e-36

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.71  E-value: 5.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGG-S 901
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI-GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQS-DARIQEPTRLVKDHNVTVLVISTLEADKNFIINLSAEN 975
Cdd:pfam00092   80 NTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEP 154
ZP super family cl42957
Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona ...
 1050-1299 1.37e-26

Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona pellucida. ZP domains are also present in multidomain transmembrane proteins such as glycoprotein GP2, uromodulin and TGF-beta receptor type III (betaglycan).


The actual alignment was detected with superfamily member smart00241:

Pssm-ID: 214579  Cd Length: 252  Bit Score: 110.17  E-value: 1.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1050 ECVGDGFKVQVNPPAGFRGVAVVKGYQD-DARCKA--TASSSLPLNLFISNNECGVtqVKSSDPNGLNSSLVLHL-LHDD 1125
Cdd:smart00241    1 QCGEDQMVVSVSTDLLFPGGINVKGLTLgDPSCRPqfTDATSAFVSFEVPLNGCGT--RRQVNPDGIVYSNTLVVsPFHP 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1126 ELNTAEDR-AYLLQCFIgaqNQDAVVSTNLNVvrSELAIAETISLSTLPPTCTYSIRKEGPEGPIV--SRAVVGQTVWHR 1202
Cdd:smart00241   79 GFITRDDRaAYHFQCFY---PENEKVSLNLDV--STIPPTELSSVSEGPLTCSYRLYKDDSFGSPYqsADYVLGDPVYHE 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1203 WECDGTNDTNqaYGIQVHSCYASD----DVERKFAFVDpRGCSSDLALLTDLTY-ADDSLTAWAASHVFNVHDAESLKFV 1277
Cdd:smart00241  154 WECDGADDPP--LGLLVDNCYATPgpdpSSGPKYFIID-NGCPVDGYLDSTIPYnSNPLHRARFSVKVFKFADRSLVYFH 230

                           250       260
                    ....*....|....*....|...
gi 1845973558  1278 CKLSLC-TRDGDGCEGvtpPACG 1299
Cdd:smart00241  231 CQIRLCdKDDGSSCDG---PACS 250
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 19-153 8.84e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.79  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   19 PVLVSSQTYDAVPIGRPFLRPPPSPRQEEAPAPTLARGYQPP---PRPSNFQPPRSYPSFRQPSLNLDNRQFPGNHQ--R 93
Cdd:pfam09770  222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQptQ 301

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   94 AGQNFNWQMQqlqqqdpqrfgfrQQQRTIPQTPPSFQPPHNHFRAGAPGQIPHQGRQVAH 153
Cdd:pfam09770  302 ILQNPNRLSA-------------ARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
823-975 5.74e-36

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.71  E-value: 5.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGG-S 901
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI-GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQS-DARIQEPTRLVKDHNVTVLVISTLEADKNFIINLSAEN 975
Cdd:pfam00092   80 NTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEP 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 822-972 6.98e-32

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 122.40  E-value: 6.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  822 TDILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNFGaDGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTG-G 900
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGP-DKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845973558  901 SQLNKALEKVSQFAFTkKRGDRPDAENILIIVTDGQSDAR--IQEPTRLVKDHNVTVLVISTLEADKNFIINLS 972
Cdd:cd01450     80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 823-994 1.22e-29

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 116.40  E-value: 1.22e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFsNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTE-FMTGGS 901
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQL-DIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQSD---ARIQEPTRLVKDHNVTVLVISTLEA-DKNFIINLSAENLY 977
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNdgpKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG 159

                           170
                    ....*....|....*..
gi 1845973558   978 DSdNFGKDLAWKLAKRI 994
Cdd:smart00327  160 VY-VFLPELLDLLIDLL 175
ZP smart00241
Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona ...
 1050-1299 1.37e-26

Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona pellucida. ZP domains are also present in multidomain transmembrane proteins such as glycoprotein GP2, uromodulin and TGF-beta receptor type III (betaglycan).


Pssm-ID: 214579  Cd Length: 252  Bit Score: 110.17  E-value: 1.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1050 ECVGDGFKVQVNPPAGFRGVAVVKGYQD-DARCKA--TASSSLPLNLFISNNECGVtqVKSSDPNGLNSSLVLHL-LHDD 1125
Cdd:smart00241    1 QCGEDQMVVSVSTDLLFPGGINVKGLTLgDPSCRPqfTDATSAFVSFEVPLNGCGT--RRQVNPDGIVYSNTLVVsPFHP 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1126 ELNTAEDR-AYLLQCFIgaqNQDAVVSTNLNVvrSELAIAETISLSTLPPTCTYSIRKEGPEGPIV--SRAVVGQTVWHR 1202
Cdd:smart00241   79 GFITRDDRaAYHFQCFY---PENEKVSLNLDV--STIPPTELSSVSEGPLTCSYRLYKDDSFGSPYqsADYVLGDPVYHE 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1203 WECDGTNDTNqaYGIQVHSCYASD----DVERKFAFVDpRGCSSDLALLTDLTY-ADDSLTAWAASHVFNVHDAESLKFV 1277
Cdd:smart00241  154 WECDGADDPP--LGLLVDNCYATPgpdpSSGPKYFIID-NGCPVDGYLDSTIPYnSNPLHRARFSVKVFKFADRSLVYFH 230

                           250       260
                    ....*....|....*....|...
gi 1845973558  1278 CKLSLC-TRDGDGCEGvtpPACG 1299
Cdd:smart00241  231 CQIRLCdKDDGSSCDG---PACS 250
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 810-960 7.44e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 52.25  E-value: 7.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  810 PTPNRPEIDRNRTDILFLLDSSDN-FTEQKFQRAIKLIGETVGQFSnfgaDGVQVSLVQYNDEPYLEFSLRKHncKKHLL 888
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYR----PRDRVGLVAFGGEAEVLLPLTRD--REALK 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  889 ADIADTEFmTGGSQLNKALEKvsqfAFTKKRGDRPDAENILIIVTDGQSDARIQEPT---RLVKDHNVTVLVIST 960
Cdd:COG1240    155 RALDELPP-GGGTPLGDALAL----ALELLKRADPARRKVIVLLTDGRDNAGRIDPLeaaELAAAAGIRIYTIGV 224
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 19-153 8.84e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.79  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   19 PVLVSSQTYDAVPIGRPFLRPPPSPRQEEAPAPTLARGYQPP---PRPSNFQPPRSYPSFRQPSLNLDNRQFPGNHQ--R 93
Cdd:pfam09770  222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQptQ 301

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   94 AGQNFNWQMQqlqqqdpqrfgfrQQQRTIPQTPPSFQPPHNHFRAGAPGQIPHQGRQVAH 153
Cdd:pfam09770  302 ILQNPNRLSA-------------ARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
823-975 5.74e-36

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.71  E-value: 5.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGG-S 901
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI-GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQS-DARIQEPTRLVKDHNVTVLVISTLEADKNFIINLSAEN 975
Cdd:pfam00092   80 NTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEP 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 822-972 6.98e-32

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 122.40  E-value: 6.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  822 TDILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNFGaDGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTG-G 900
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGP-DKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845973558  901 SQLNKALEKVSQFAFTkKRGDRPDAENILIIVTDGQSDAR--IQEPTRLVKDHNVTVLVISTLEADKNFIINLS 972
Cdd:cd01450     80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 823-994 1.22e-29

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 116.40  E-value: 1.22e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFsNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTE-FMTGGS 901
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQL-DIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQSD---ARIQEPTRLVKDHNVTVLVISTLEA-DKNFIINLSAENLY 977
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNdgpKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG 159

                           170
                    ....*....|....*..
gi 1845973558   978 DSdNFGKDLAWKLAKRI 994
Cdd:smart00327  160 VY-VFLPELLDLLIDLL 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 822-966 1.14e-28

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 113.48  E-value: 1.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  822 TDILFLLDSSDNFTEQKFQRAIKLIGETVGQFsNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGGS 901
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERL-DIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQSDARIQEPTRLVKDHNVTVLVISTLEADKN 966
Cdd:cd01472     80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEE 144
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 822-966 2.39e-28

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 112.38  E-value: 2.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  822 TDILFLLDSSDNFTEQKFQRAIKLIGETVGQFsNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGGS 901
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQSDARIQEPTRLVKDHNVTVLVISTLEADKN 966
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADES 144
ZP smart00241
Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona ...
 1050-1299 1.37e-26

Zona pellucida (ZP) domain; ZP proteins are responsible for sperm-adhesion fo the zona pellucida. ZP domains are also present in multidomain transmembrane proteins such as glycoprotein GP2, uromodulin and TGF-beta receptor type III (betaglycan).


Pssm-ID: 214579  Cd Length: 252  Bit Score: 110.17  E-value: 1.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1050 ECVGDGFKVQVNPPAGFRGVAVVKGYQD-DARCKA--TASSSLPLNLFISNNECGVtqVKSSDPNGLNSSLVLHL-LHDD 1125
Cdd:smart00241    1 QCGEDQMVVSVSTDLLFPGGINVKGLTLgDPSCRPqfTDATSAFVSFEVPLNGCGT--RRQVNPDGIVYSNTLVVsPFHP 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1126 ELNTAEDR-AYLLQCFIgaqNQDAVVSTNLNVvrSELAIAETISLSTLPPTCTYSIRKEGPEGPIV--SRAVVGQTVWHR 1202
Cdd:smart00241   79 GFITRDDRaAYHFQCFY---PENEKVSLNLDV--STIPPTELSSVSEGPLTCSYRLYKDDSFGSPYqsADYVLGDPVYHE 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  1203 WECDGTNDTNqaYGIQVHSCYASD----DVERKFAFVDpRGCSSDLALLTDLTY-ADDSLTAWAASHVFNVHDAESLKFV 1277
Cdd:smart00241  154 WECDGADDPP--LGLLVDNCYATPgpdpSSGPKYFIID-NGCPVDGYLDSTIPYnSNPLHRARFSVKVFKFADRSLVYFH 230

                           250       260
                    ....*....|....*....|...
gi 1845973558  1278 CKLSLC-TRDGDGCEGvtpPACG 1299
Cdd:smart00241  231 CQIRLCdKDDGSSCDG---PACS 250
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 823-966 4.38e-20

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 88.92  E-value: 4.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQrAIKLIGETVGQFSNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMtGGSQ 902
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFP-AIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLR-GGSQ 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845973558  903 LN--KALEKVSQFAFTKKRGDRPdAENI---LIIVTDGQSDARIQEPTRLVKDHNVTVLVISTLEADKN 966
Cdd:cd01481     80 LNtgSALDYVVKNLFTKSAGSRI-EEGVpqfLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLA 147
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 823-958 5.36e-16

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 76.84  E-value: 5.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMT-GGS 901
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSA-SPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  902 QLNKALEKVSQFAftkKRGDRPDAENILIIVTDGQSDARIQEPTRLV---KDHNVTVLVI 958
Cdd:cd00198     81 NIGAALRLALELL---KSAKRPNARRVIILLTDGEPNDGPELLAEAArelRKLGITVYTI 137
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 822-937 2.00e-15

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 75.86  E-value: 2.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  822 TDILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGGS 901
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDI-GPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1845973558  902 QLNKALEKVSQFAFTKKRGDRPDAENILIIVTDGQS 937
Cdd:cd01469     80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGES 115
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 821-966 7.80e-15

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 75.50  E-value: 7.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  821 RTDILFLLDSSDNFTEQKFQRAIKLIGETVgQFSNFGADGVQVSLVQYNDEPYLEFSLRKHNCKKHLLADIADTEFMTGG 900
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQII-DSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845973558  901 SQLNKALEKVSQFAFTKKRGDRPDAENI---LIIVTDGQSDARIQEPTRLVKDHNVTVLVISTLEADKN 966
Cdd:cd01475     81 TMTGLAIQYAMNNAFSEAEGARPGSERVprvGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEE 149
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 823-946 4.64e-12

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 65.50  E-value: 4.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNfTEQKFQRAIKLIGETVGQFSNfGADGVQVSLVQYNDEP--YLEFSLRKHNCKKHLLADIADTEFMTGG 900
Cdd:cd01476      2 DLLFVLDSSGS-VRGKFEKYKKYIERIVEGLEI-GPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1845973558  901 SQLNKALEKVSQFaFTKKRGDRPDAENILIIVTDGQSDARIQEPTR 946
Cdd:cd01476     80 TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQAR 124
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 823-983 5.45e-10

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 60.09  E-value: 5.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQKFQRAIKLIGETVGQFSNFG-----ADGVQVSLVQYNDEPYLEF-SLRKHNCKKHLLADIADTEF 896
Cdd:cd01480      4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYyrkdpAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  897 MTGGSQLNKALEKVSQFAftkKRGDRPDAENILIIVTDGQSDAR--------IQEPTRL-VKDHnvtVLVISTLEADKNF 967
Cdd:cd01480     84 IGGGTFTDCALKYATEQL---LEGSHQKENKFLLVITDGHSDGSpdggiekaVNEADHLgIKIF---FVAVGSQNEEPLS 157

                          170
                   ....*....|....*..
gi 1845973558  968 IINLSA-ENLYDSdNFG 983
Cdd:cd01480    158 RIACDGkSALYRE-NFA 173
VWA_2 pfam13519
von Willebrand factor type A domain;
824-932 1.56e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.53  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  824 ILFLLDSS-----DNFTEQKFQRAIKLIGETVGQFsnfgaDGVQVSLVQYNDEPYLEFSLRKHncKKHLLADIADTEFMT 898
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSL-----PGDRVGLVTFGDGPEVLIPLTKD--RAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1845973558  899 GGSQLNKALEKVSQFAFTkkrgDRPDAENILIIV 932
Cdd:pfam13519   74 GGTNLAAALQLARAALKH----RRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 823-959 4.45e-08

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 54.70  E-value: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  823 DILFLLDSSDNFTEQ-KFQRAIKLIGETVGQFsNFGADGVQVSLVQYNDEPYLEFSLRKHNCK-----KHLLADIADTEF 896
Cdd:cd01471      2 DLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNL-NISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  897 MTGGSQLNKALEKVSQFAFTKkRGDRPDAENILIIVTDGQSDARIQ--EPTRLVKDHNVTVLVIS 959
Cdd:cd01471     81 PNGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLG 144
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 810-960 7.44e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 52.25  E-value: 7.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558  810 PTPNRPEIDRNRTDILFLLDSSDN-FTEQKFQRAIKLIGETVGQFSnfgaDGVQVSLVQYNDEPYLEFSLRKHncKKHLL 888
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYR----PRDRVGLVAFGGEAEVLLPLTRD--REALK 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845973558  889 ADIADTEFmTGGSQLNKALEKvsqfAFTKKRGDRPDAENILIIVTDGQSDARIQEPT---RLVKDHNVTVLVIST 960
Cdd:COG1240    155 RALDELPP-GGGTPLGDALAL----ALELLKRADPARRKVIVLLTDGRDNAGRIDPLeaaELAAAAGIRIYTIGV 224
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 19-153 8.84e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.79  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   19 PVLVSSQTYDAVPIGRPFLRPPPSPRQEEAPAPTLARGYQPP---PRPSNFQPPRSYPSFRQPSLNLDNRQFPGNHQ--R 93
Cdd:pfam09770  222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQptQ 301

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973558   94 AGQNFNWQMQqlqqqdpqrfgfrQQQRTIPQTPPSFQPPHNHFRAGAPGQIPHQGRQVAH 153
Cdd:pfam09770  302 ILQNPNRLSA-------------ARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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